REFERENCES



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Kasprowicz A, Spriet C, Terryn C, Rigolot V, Hardiville S, Alteen MG, Lefebvre T, Biot C. Exploring the Potential of β-Catenin O-GlcNAcylation by Using Fluorescence-Based Engineering and Imaging. Molecules (Basel, Switzerland) 2020 25(19) 33019562
Abstract:
Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs). We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells. We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay. We validated this technology by imaging the O-GlcNAcylation status of β-catenin in HeLa cells. The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). Finally, we provided a flowchart demonstrating how this technology is transposable to any kind of glycosylation.
O-GlcNAc proteins:
CTNB1
Species: Homo sapiens
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Masclef L, Dehennaut V, Mortuaire M, Schulz C, Leturcq M, Lefebvre T, Vercoutter-Edouart AS. Cyclin D1 Stability Is Partly Controlled by O-GlcNAcylation. Frontiers in endocrinology 2019 10 30853938
Abstract:
Cyclin D1 is the regulatory partner of the cyclin-dependent kinases (CDKs) CDK4 or CDK6. Once associated and activated, the cyclin D1/CDK complexes drive the cell cycle entry and G1 phase progression in response to extracellular signals. To ensure their timely and accurate activation during cell cycle progression, cyclin D1 turnover is finely controlled by phosphorylation and ubiquitination. Here we show that the dynamic and reversible O-linked β-N-Acetyl-glucosaminylation (O-GlcNAcylation) regulates also cyclin D1 half-life. High O-GlcNAc levels increase the stability of cyclin D1, while reduction of O-GlcNAcylation strongly decreases it. Moreover, elevation of O-GlcNAc levels through O-GlcNAcase (OGA) inhibition significantly slows down the ubiquitination of cyclin D1. Finally, biochemical and cell imaging experiments in human cancer cells reveal that the O-GlcNAc transferase (OGT) binds to and glycosylates cyclin D1. We conclude that O-GlcNAcylation promotes the stability of cyclin D1 through modulating its ubiquitination.
O-GlcNAc proteins:
CCND1
Species: Homo sapiens
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Biwi J, Clarisse C, Biot C, Kozak RP, Madunic K, Mortuaire M, Wuhrer M, Spencer DIR, Schulz C, Guerardel Y, Lefebvre T, Vercoutter-Edouart AS. OGT Controls the Expression and the Glycosylation of E-cadherin, and Affects Glycosphingolipid Structures in Human Colon Cell Lines. Proteomics 2019 19(21-22) 31373757
Abstract:
Colorectal cancer (CRC) affects both women and men living in societies with a high sedentary lifestyle. Amongst the phenotypic changes exhibited by tumor cells, a wide range of glycosylation has been reported for colon cancer-derived cell lines and CRC tissues. These aberrant modifications affect different aspects of glycosylation, including an increase in core fucosylation and GlcNAc branching on N-glycans, alteration of O-glycans, upregulated sialylation, and O-GlcNAcylation. Although O-GlcNAcylation and complex glycosylations differ in many aspects, sparse evidences report on the interference of O-GlcNAcylation with complex glycosylation. Nevertheless, this relationship is still a matter of debate. Combining different approaches on three human colon cell lines (HT29, HCT116 and CCD841CoN), it is herein reported that silencing O-GlcNAc transferase (OGT, the sole enzyme driving O-GlcNAcylation), only slightly affects overall N- and O-glycosylation patterns. Interestingly, silencing of OGT in HT29 cells upregulates E-cadherin (a major actor of epithelial-to-mesenchymal transition) and changes its glycosylation. On the other hand, OGT silencing perturbs biosynthesis of glycosphingolipids resulting in a decrease in gangliosides and an increase in globosides. Together, these results provide novel insights regarding the selective regulation of complex glycosylations by O-GlcNAcylation in colon cancer cells.
O-GlcNAc proteins:
CADH1
Species: Homo sapiens
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Torres-Gutiérrez E, Pérez-Cervera Y, Camoin L, Zenteno E, Aquino-Gil MO, Lefebvre T, Cabrera-Bravo M, Reynoso-Ducoing O, Bucio-Torres MI, Salazar-Schettino PM. Identification of O-Glcnacylated Proteins in Trypanosoma cruzi. Frontiers in endocrinology 2019 10 30984116
Abstract:
Originally an anthropozoonosis in the Americas, Chagas disease has spread from its previous borders through migration. It is caused by the protozoan Trypanosoma cruzi. Differences in disease severity have been attributed to a natural pleomorphism in T. cruzi. Several post-translational modifications (PTMs) have been studied in T. cruzi, but to date no work has focused on O-GlcNAcylation, a highly conserved monosaccharide-PTM of serine and threonine residues mainly found in nucleus, cytoplasm, and mitochondrion proteins. O-GlcNAcylation is thought to regulate protein function analogously to protein phosphorylation; indeed, crosstalk between both PTMs allows the cell to regulate its functions in response to nutrient levels and stress. Herein, we demonstrate O-GlcNAcylation in T. cruzi epimastigotes by three methods: by using specific antibodies against the modification in lysates and whole parasites, by click chemistry labeling, and by proteomics. In total, 1,271 putative O-GlcNAcylated proteins and six modification sequences were identified by mass spectrometry (data available via ProteomeXchange, ID PXD010285). Most of these proteins have structural and metabolic functions that are essential for parasite survival and evolution. Furthermore, O-GlcNAcylation pattern variations were observed by antibody detection under glucose deprivation and heat stress conditions, supporting their possible role in the adaptive response. Given the numerous biological processes in which O-GlcNAcylated proteins participate, its identification in T. cruzi proteins opens a new research field in the biology of Trypanosomatids, improve our understanding of infection processes and may allow us to identify new therapeutic targets.
O-GlcNAc proteins:
A0A0F6YF08, A0A0M3NVD0, A0A0M3YBC4, A0A189XHE2, A0A1B1R0W9, A0A286R981, A0SZK3, A5JUX3, A6N830, A7UL80, B3U4H3, B5U6U4, C9DS87, D1LWU5, D9I8N9, G0Z187, G4WJW3, G8FL60, H9AZG3, H9AZH1, H9AZH6, H9M3L8, I3QF27, J3JZZ0, K2LUZ2, K2LV71, K2LVR5, K2LVZ1, K2LXG1, K2LY59, K2LY67, K2LYT1, K2LZ01, K2M094, K2M439, K2M491, K2M4M1, K2M4S3, K2M518, K2M526, K2M5Q0, K2M5Q3, K2M5W0, K2M603, K2M6U1, K2M6U4, K2M741, K2M7F4, K2M7Z5, K2M842, K2M892, K2M9C4, K2M9U9, K2MA70, K2MAF9, K2MAY5, K2MAZ3, K2MCN3, K2MCT5, K2MCY1, K2MDE9, K2MDJ7, K2MEB2, K2MHI4, K2MI51, K2MK39, K2MKM4, K2MKU0, K2MLW4, K2MM88, K2MN29, K2MN89, K2MNC2, K2MNF2, K2MNK2, K2MNZ2, K2MPW1, K2MQ45, K2MQ55, K2MQY7, K2MR15, K2MRQ3, K2MRY2, K2MSQ3, K2MSW9, K2MT40, K2MTF7, K2MTH2, K2MU46, K2MUF1, K2MUS2, K2MVC2, K2MVK4, K2MVP9, K2MVW9, K2MVZ1, K2MW43, K2MW55, K2MWA1, K2MWQ0, K2MWX3, K2MWY1, K2MX11, K2MXC9, K2MXG0, K2MXN7, K2MXT6, K2MXY3, K2MY44, K2MY82, K2MYH5, K2MYY2, K2MZ11, K2MZF4, K2MZF5, K2MZJ0, K2MZL9, K2N002, K2N008, K2N040, K2N084, K2N0A2, K2N0N5, K2N0W4, K2N128, K2N161, K2N1L0, K2N1M9, K2N200, K2N232, K2N279, K2N4P9, K2N598, K2N5B4, K2N5L9, K2N5P8, K2N5S2, K2N5W3, K2N683, K2N687, K2N6G2, K2N6M0, K2N6V1, K2N704, K2N8E5, K2N987, K2N9B5, K2NA63, K2NAE4, K2NAH8, K2NBJ9, K2NBK1, K2NC20, K2NC76, K2NC82, K2NC88, K2NCV2, K2NE71, K2NE72, K2NE80, K2NES1, K2NEY2, K2NFF1, K2NG18, K2NGH9, K2NGI2, K2NGT6, K2NH93, K2NHB5, K2NIQ0, K2NJ61, K2NJG1, K2NJM5, K2NJP3, K2NJP7, K2NL34, K2NLA3, K2NLJ5, K2NLK6, K2NLQ2, K2NMM5, K2NNM1, K2NP04, K2NP31, K2NQC5, K2NRA3, K2NSB8, K2NSH4, K2NSL2, K2NSP8, K2NSS5, K2NTN6, K2NVY6, K2NW21, K2NW49, K2NW93, K2NWK7, K2NX50, K2P6Y7, K2P9C9, K2PAY9, K2PBQ1, K2PCH2, K2PCJ0, K2PDG2, K2PDY3, K2PE13, K2PFE2, K4E123, K7SWG8, K7ZR76, M4H1F5, M4H1T0, M4H2K1, RL28, O15637, O60947, O60996, O61066, O61083, O61084, O62594, O76138, O77252, O79469, O96673, TCP17, HSP70, HSP85, RL402, G3PG, TCNA, RLA1, ATTY, TPIS, PSA1, Q003G7, Q1WBU6, Q26858, Q26887, Q26936, Q26944, Q26947, Q26952, Q27791, Q27796, Q2I5R9, Q2TJ65, Q3ZMB7, Q49UB9, Q4CKT7, Q4CLI0, Q4CLM5, Q4CLN1, Q4CLP6, Q4CLQ9, Q4CLR4, Q4CLV8, Q4CLW3, Q4CLY6, Q4CM27, Q4CM56, Q4CM68, Q4CM72, Q4CM73, Q4CMA6, Q4CME2, Q4CMM4, Q4CMR1, Q4CMS5, Q4CMT2, Q4CMU8, Q4CN66, Q4CN82, Q4CNC6, Q4CNF4, Q4CNM5, Q4CNU0, Q4CP05, Q4CP06, Q4CP28, Q4CP43, Q4CP89, Q4CP97, Q4CPE2, Q4CPG3, Q4CPG4, Q4CPJ3, Q4CPK3, Q4CPK8, Q4CPM5, Q4CPP0, Q4CPR5, Q4CPU3, Q4CPV9, Q4CPW5, Q4CQ34, Q4CQ46, Q4CQ54, Q4CQ63, Q4CQ81, Q4CQA1, Q4CQG0, Q4CQI9, Q4CQM4, Q4CQR0, Q4CQX2, Q4CR06, Q4CR09, Q4CR35, Q4CR84, Q4CRA7, Q4CRH9, Q4CRK6, Q4CRM4, Q4CRM5, Q4CRN7, Q4CRN8, Q4CRQ6, Q4CRR1, Q4CRT0, Q4CRU8, Q4CRX5, Q4CS11, Q4CS16, Q4CS20, Q4CS26, Q4CS27, Q4CS80, Q4CS87, Q4CSD4, Q4CSD9, Q4CSI4, Q4CSI8, Q4CSK3, Q4CSK4, Q4CSL1, Q4CSL9, Q4CSN9, Q4CSR6, Q4CSR8, Q4CSV9, Q4CSY5, Q4CT37, Q4CTC0, Q4CTD7, Q4CTE7, Q4CTG8, Q4CTK4, Q4CTP1, Q4CTS3, Q4CTS4, Q4CTV7, Q4CU52, Q4CU59, Q4CU61, Q4CU72, Q4CU74, Q4CU77, Q4CU84, Q4CU91, Q4CU92, Q4CUC8, Q4CUE0, Q4CUF9, Q4CUL1, Q4CUV9, Q4CUW8, Q4CUZ7, Q4CV48, Q4CV87, Q4CVC6, Q4CVE1, Q4CVG3, Q4CVJ1, Q4CVJ2, Q4CVJ7, Q4CVL1, Q4CVP1, Q4CVQ3, Q4CVR9, Q4CVT7, Q4CVW3, Q4CVX7, Q4CVX9, Q4CW02, Q4CW22, Q4CW23, Q4CW28, Q4CW30, Q4CW52, Q4CW64, Q4CWE3, Q4CWE6, Q4CWM5, Q4CWM6, Q4CWN9, Q4CWQ8, Q4CWR1, Q4CWT2, Q4CWY3, Q4CX80, Q4CXC3, Q4CXE1, Q4CXE8, Q4CXI6, Q4CXJ4, Q4CXJ6, Q4CXJ7, Q4CXK2, Q4CXN4, Q4CXN8, Q4CXQ1, Q4CXR7, Q4CXR9, Q4CXV1, Q4CXW2, Q4CXW9, Q4CXX9, Q4CY01, Q4CY08, Q4CY21, Q4CY42, Q4CY95, Q4CYA5, Q4CYC6, Q4CYE2, Q4CYE8, Q4CYG8, Q4CYH9, Q4CYL3, Q4CYN4, Q4CYN6, Q4CYR3, Q4CYW6, Q4CYZ1, Q4CYZ6, Q4CZ11, Q4CZ35, Q4CZB7, Q4CZF0, Q4CZF4, Q4CZG5, Q4CZK3, Q4CZK9, Q4CZQ3, Q4CZQ7, Q4CZR0, Q4CZT6, Q4CZV4, Q4CZX4, Q4CZY1, Q4CZZ3, Q4D049, Q4D059, Q4D066, Q4D078, Q4D083, Q4D085, Q4D0A7, Q4D0A9, Q4D0C0, Q4D0E4, Q4D0K8, Q4D0M6, Q4D0R4, Q4D0S6, Q4D0U5, Q4D0W7, Q4D0X1, Q4D139, Q4D144, Q4D157, Q4D189, Q4D193, Q4D1D3, Q4D1I7, Q4D1P9, Q4D1Q4, Q4D1R0, Q4D1V7, Q4D1Y5, Q4D1Y7, Q4D205, Q4D214, Q4D276, Q4D2D7, Q4D2I4, Q4D2R8, RS3A1, Q4D2T0, Q4D2X1, Q4D2Z8, Q4D3A9, DRE21, Q4D3E3, Q4D3H6, Q4D3T1, Q4D3V3, PYRD, Q4D3W7, Q4D425, Q4D436, Q4D487, Q4D4E6, Q4D4F5, Q4D4L3, Q4D4M0, Q4D4M2, Q4D4N6, Q4D4R0, Q4D4R9, Q4D4S1, Q4D4V5, Q4D4X1, Q4D4X6, ECOT2, Q4D4Y8, Q4D4Z3, Q4D518, Q4D528, Q4D546, Q4D578, Q4D579, Q4D588, Q4D590, Q4D5C1, Q4D5E8, Q4D5R2, Q4D5T6, Q4D5V2, Q4D5X2, Q4D5Z3, Q4D630, Q4D6D8, Q4D6F1, Q4D6H3, Q4D6I3, Q4D6I5, Q4D6J0, Q4D6M9, Q4D6N5, Q4D6P0, Q4D6P2, Q4D6Q6, Q4D6V2, Q4D6Z3, Q4D722, Q4D747, Q4D751, Q4D758, Q4D779, Q4D795, Q4D7A0, Q4D7D2, Q4D7D9, Q4D7G9, Q4D7L3, Q4D7P6, Q4D7T7, Q4D7X5, Q4D820, Q4D823, Q4D864, Q4D866, Q4D867, Q4D8B1, Q4D8D3, Q4D8D7, Q4D8J9, Q4D8K3, Q4D8S5, Q4D8U0, Q4D930, Q4D966, Q4D968, Q4D9B4, Q4D9F7, Q4D9H3, Q4D9L7, Q4D9M6, Q4D9P7, Q4D9Q4, Q4D9Q8, Q4D9Q9, Q4D9S6, Q4D9S8, Q4D9Z1, Q4D9Z2, Q4D9Z9, Q4DA08, Q4DA32, Q4DA33, Q4DA54, Q4DA86, Q4DAD2, Q4DAE1, Q4DAF0, Q4DAG5, Q4DAK5, Q4DAN2, Q4DAP4, Q4DAU6, Q4DAV0, Q4DAV1, Q4DAX6, Q4DAY6, Q4DAZ6, Q4DB19, Q4DB46, Q4DB81, Q4DBB6, Q4DBC5, Q4DBG8, Q4DBH3, Q4DBL6, Q4DBP4, Q4DBR1, Q4DBS8, Q4DBV1, Q4DBY3, Q4DC00, Q4DC38, Q4DC65, Q4DCA9, Q4DCC6, Q4DCH7, Q4DCI2, Q4DCI5, Q4DCL6, Q4DCM3, Q4DCN7, Q4DCQ5, Q4DCV7, Q4DCX1, Q4DCY3, Q4DD18, Q4DD50, Q4DD81, Q4DDC1, Q4DDH1, Q4DDI3, Q4DDI8, Q4DDK6, Q4DDL0, Q4DDN8, Q4DDP3, Q4DDS8, Q4DDT6, Q4DDW5, Q4DDZ3, Q4DE00, Q4DE24, Q4DE31, Q4DE50, Q4DE52, Q4DE75, Q4DE88, Q4DEA8, Q4DEC1, Q4DEC2, Q4DED2, Q4DED3, Q4DEE6, Q4DEE8, Q4DEI2, Q4DEJ1, Q4DEJ6, Q4DEM5, Q4DER7, Q4DES9, Q4DET0, Q4DF18, Q4DF20, Q4DF36, Q4DF59, Q4DFA8, Q4DFB8, Q4DFD2, Q4DFE2, Q4DFF8, Q4DFG3, Q4DFI8, Q4DFJ5, Q4DFL2, Q4DFM2, Q4DFP0, Q4DFP8, Q4DFR9, Q4DFY0, Q4DG00, Q4DG03, Q4DG06, Q4DG22, Q4DG40, Q4DG45, Q4DG60, Q4DG63, Q4DG77, Q4DG96, Q4DGA2, Q4DGE9, Q4DGL9, Q4DGP8, Q4DGP9, Q4DGT9, Q4DGU2, Q4DGW6, Q4DH63, Q4DH94, Q4DHB2, Q4DHC6, Q4DHD3, Q4DHD9, Q4DHG7, Q4DHI7, Q4DHL4, Q4DHP0, Q4DHP4, Q4DHP8, Q4DHS8, Q4DHY1, Q4DI05, Q4DI68, Q4DI85, Q4DIB5, Q4DIB9, Q4DIF6, Q4DIG2, Q4DIJ8, Q4DIR3, Q4DIR4, Q4DIX2, Q4DIX3, Q4DJ19, Q4DJ30, Q4DJ36, Q4DJ40, Q4DJ42, Q4DJ49, Q4DJ96, Q4DJA1, Q4DJC9, Q4DJD0, Q4DJF1, Q4DJN0, Q4DJN8, Q4DJQ5, Q4DJQ7, Q4DJR7, Q4DJT8, Q4DJX1, Q4DJZ1, Q4DJZ9, Q4DK31, Q4DK73, Q4DK88, Q4DKG4, Q4DKI5, Q4DKK5, Q4DKQ2, Q4DKT2, Q4DKU5, Q4DKU9, Q4DKX0, Q4DKY2, Q4DKY7, Q4DKY8, Q4DKZ4, Q4DL24, Q4DL81, Q4DL82, Q4DLB9, Q4DLH1, Q4DLI2, Q4DLL1, Q4DLM5, Q4DLN7, Q4DLU4, Q4DLY6, Q4DLZ0, Q4DM53, Q4DM59, Q4DM81, Q4DM82, Q4DM83, Q4DME7, Q4DME9, Q4DMG9, Q4DMH1, Q4DMH3, Q4DMK9, Q4DMU8, Q4DMU9, Q4DMV1, Q4DMW3, Q4DMX9, Q4DN30, Q4DN34, Q4DNB9, Q4DNL0, Q4DNM4, Q4DNR3, Q4DNU7, Q4DP31, Q4DP48, Q4DPB6, Q4DPC8, Q4DPE4, Q4DPH7, Q4DPH9, Q4DPI6, Q4DPL8, Q4DPM2, Q4DPP9, Q4DPQ9, Q4DPR3, Q4DPS5, Q4DPS6, Q4DPV6, Q4DPV9, Q4DPX8, Q4DPZ5, Q4DQ27, Q4DQ35, Q4DQ37, Q4DQ63, Q4DQ86, Q4DQJ3, Q4DQQ7, Q4DQS9, Q4DQT6, Q4DQV3, Q4DQZ1, Q4DR16, Q4DR33, Q4DR82, Q4DRB5, Q4DRE9, Q4DRF1, Q4DRF5, Q4DRJ9, Q4DRK8, Q4DRL1, Q4DRN5, Q4DRW8, Q4DS83, Q4DSA0, Q4DSE6, Q4DSF3, Q4DSI2, Q4DSI7, Q4DSJ1, Q4DSL1, Q4DSM6, Q4DSP6, Q4DSP9, Q4DST2, Q4DST7, Q4DSU6, Q4DSW2, Q4DSW8, Q4DSZ1, Q4DSZ8, Q4DT66, Q4DT70, Q4DT78, Q4DTA0, Q4DTD7, Q4DTE0, Q4DTE6, Q4DTE8, Q4DTE9, Q4DTI1, Q4DTI4, Q4DTJ6, Q4DTQ1, Q4DTR0, Q4DTR8, Q4DTU3, Q4DTU8, Q4DTW1, Q4DTX5, Q4DU38, Q4DU59, Q4DU60, Q4DU83, Q4DU88, Q4DUB8, Q4DUD1, Q4DUD6, Q4DUF6, Q4DUG1, Q4DUH1, Q4DUI3, Q4DUK6, Q4DUM4, Q4DUP6, Q4DUP9, Q4DUR6, Q4DUT9, Q4DUU1, Q4DUW5, Q4DUX1, Q4DUX9, Q4DV13, Q4DV14, Q4DV61, Q4DV75, Q4DV93, Q4DVF8, Q4DVG6, Q4DVM9, Q4DVV0, Q4DW27, Q4DW33, Q4DW38, Q4DW49, Q4DW59, Q4DW67, Q4DW83, Q4DWB5, Q4DWC3, Q4DWC5, Q4DWD1, Q4DWI0, Q4DWK5, Q4DWN4, Q4DWS5, Q4DWX5, Q4DWX7, Q4DWX8, Q4DWY3, Q4DX01, Q4DX64, Q4DX67, Q4DX76, Q4DX81, Q4DXC5, Q4DXK1, Q4DXK6, Q4DXK7, Q4DXR1, Q4DXW6, Q4DXW9, Q4DXX0, Q4DXX2, Q4DXX9, Q4DXY6, Q4DY15, Q4DY42, Q4DY45, Q4DY53, Q4DY80, Q4DYE0, Q4DYG1, Q4DYH1, Q4DYH2, Q4DYH7, Q4DYH8, Q4DYL9, Q4DYP1, Q4DYP5, Q4DYQ9, Q4DYS1, Q4DYS2, Q4DYS3, Q4DYW4, Q4DZ02, Q4DZ63, Q4DZ97, Q4DZ98, Q4DZ99, Q4DZB0, Q4DZC9, Q4DZF5, Q4DZJ8, Q4DZK7, Q4DZM2, Q4DZM9, Q4DZN7, RL18, Q4DZP3, Q4DZQ8, Q4DZR2, Q4DZR8, Q4DZT1, Q4DZU7, Q4DZW1, Q4E025, Q4E085, Q4E087, Q4E088, Q4E093, IF61, Q4E0C2, Q4E0D4, Q4E0F9, Q4E0G0, Q4E0G8, Q4E0G9, Q4E0K0, Q4E0L0, Q4E0M2, Q4E0P7, Q4E0P9, Q4E0Q6, Q4E0R0, Q4E0R4, Q4E0T1, Q4E0Y0, Q4E0Y2, Q4E121, Q4E133, IF4A, Q4E1B7, Q4E1D4, Q4E1M3, Q4E1N1, Q4E1R5, Q4E1X0, Q4E1X1, Q4E256, Q4E2D6, Q4E2E5, Q4E2I6, Q4E2J8, Q4E2Q9, Q4E2T9, Q4E2U5, Q4E2V9, Q4E2Y1, Q4E322, Q4E333, Q4E340, Q4E342, Q4E396, Q4E3F7, Q4E3H4, Q4E3J6, Q4E3K5, Q4E3L2, Q4E3M6, Q4E3N3, Q4E3P1, Q4E3W1, Q4E3Y5, Q4E4E9, Q4E4L7, Q4E4N4, Q4E4N6, Q4E4N8, Q4E4P6, Q4E4Q8, Q4E4R0, Q4E4S2, Q4E4T3, Q4E4T4, Q4E4V2, Q4E4W2, Q4E544, Q4E581, Q4E585, Q4E5A0, Q4E5D6, Q4E5G9, Q4E5H0, Q4E5I4, Q4E5Z1, Q4E602, Q4E617, Q4E642, Q4E650, Q4E663, Q58XP3, Q5EFD2, Q670S5, Q6B9P3, Q6BCB3, Q6QR20, Q6QT30, Q6WAT4, Q6XD84, Q6Y8Q6, Q6ZXB9, Q7YUF0, Q7YZX6, Q7Z1X0, Q869B2, Q8I6L9, Q8I728, Q8MZQ5, Q8STF3, Q8T7V6, Q8T8E0, Q8T8E2, Q8T9X5, Q8WQR2, Q8WR03, Q8WTN6, Q94798, Q95WZ9, Q9GN79, Q9GU99, Q9NG30, Q9U664, Q9U681, Q9XY64, V5A3P8, V5A4R3, V5AIW7, V5AJF7, V5AJG2, V5AJP3, V5AK68, V5AKF9, V5AKS1, V5AKY1, V5ALW0, V5AMP1, V5AMR3, V5AN41, V5ANE6, V5ANS4, V5AP12, V5AP89, V5APL8, V5APV8, V5AQ73, V5AQR9, V5AQX9, V5AR01, V5AR23, V5ARJ3, V5ARP0, V5ARR9, V5ARU0, V5ARY9, V5AS37, V5AS61, V5AS75, V5AS93, V5ASA0, V5ASA4, V5ASD7, V5ASG2, V5ASI1, V5ASP0, V5ASS1, V5ASV7, V5AT23, V5AT58, V5AT73, V5ATK8, V5ATR8, V5ATY0, V5ATY2, V5ATY5, V5AU06, V5AU76, V5AUA2, V5AUE3, V5AUF3, V5AUH1, V5AUI9, V5AUM3, V5AUS2, V5AUU0, V5AUX6, V5AV12, V5AV92, V5AVB0, V5AVG5, V5AVH4, V5AVM2, V5AVR5, V5AVV7, V5AW68, V5AW74, V5AW77, V5AWB3, V5AWC6, V5AWD8, V5AWF3, V5AWG2, V5AWT4, V5AWV1, V5AX22, V5AXC5, V5AXK4, V5AXL0, V5AXL4, V5AXN2, V5AXY2, V5AXZ0, V5AY06, V5AY62, V5AYD4, V5AYL6, V5AYP7, V5AYZ4, V5AZ01, V5AZ02, V5AZ24, V5AZ52, V5AZ66, V5AZB4, V5AZD0, V5AZD5, V5AZQ0, V5AZT5, V5AZY0, V5B059, V5B0C7, V5B0F3, V5B0K2, V5B0M9, V5B0Q8, V5B0R0, V5B0S4, V5B0W6, V5B0Z2, V5B117, V5B145, V5B1G9, V5B1P3, V5B1R9, V5B1V6, V5B1X4, V5B239, V5B262, V5B283, V5B2B1, V5B2B3, V5B2G2, V5B2J6, V5B2K0, V5B2L9, V5B2Y1, V5B305, V5B314, V5B346, V5B384, V5B398, V5B3D2, V5B3K7, V5B3M4, V5B3P7, V5B3T2, V5B3T7, V5B3W9, V5B400, V5B409, V5B4D8, V5B4G0, V5B4G8, V5B4K7, V5B4M0, V5B4N0, V5B4S5, V5B4S9, V5B4U5, V5B4V3, V5B4X4, V5B525, V5B579, V5B5A2, V5B5B2, V5B5E2, V5B5G8, V5B5I4, V5B5L8, V5B5N3, V5B5P0, V5B5Q0, V5B5Q5, V5B5S3, V5B5S8, V5B5X1, V5B5X6, V5B664, V5B673, V5B685, V5B6A1, V5B6F9, V5B6G9, V5B6H7, V5B6K3, V5B6M0, V5B6M4, V5B6P6, V5B6Q5, V5B6R2, V5B6S6, V5B6T4, V5B747, V5B755, V5B760, V5B765, V5B773, V5B774, V5B780, V5B793, V5B7B8, V5B7C8, V5B7G2, V5B7L4, V5B7P7, V5B7Q3, V5B7Q9, V5B7R2, V5B7Z4, V5B825, V5B836, V5B849, V5B873, V5B887, V5B8E5, V5B8F4, V5B8G2, V5B8I0, V5B8I8, V5B8K6, V5B8L2, V5B8L7, V5B8M0, V5B8M1, V5B8M5, V5B8N1, V5B8T8, V5B8T9, V5B8U8, V5B8X2, V5B8Z7, V5B8Z9, V5B920, V5B924, V5B929, V5B941, V5B985, V5B995, V5B9A3, V5B9B2, V5B9D8, V5B9E8, V5B9G3, V5B9G7, V5B9J3, V5B9S2, V5B9T6, V5B9Y2, V5BA05, V5BA48, V5BA86, V5BA93, V5BAB9, V5BAD3, V5BAE3, V5BAE8, V5BAG8, V5BAI3, V5BAK3, V5BAK4, V5BAL2, V5BAN9, V5BAP6, V5BAR1, V5BAR9, V5BAT7, V5BAU0, V5BAU6, V5BAV1, V5BAX9, V5BAY3, V5BAZ8, V5BB16, V5BB27, V5BB32, V5BB41, V5BB58, V5BB69, V5BB90, V5BBC2, V5BBD6, V5BBD7, V5BBE3, V5BBG5, V5BBJ9, V5BBM5, V5BBP4, V5BBQ7, V5BBR4, V5BBS9, V5BBU5, V5BBU8, V5BBX1, V5BBX7, V5BBY0, V5BC23, V5BC27, V5BC28, V5BC36, V5BC49, V5BC94, V5BCB8, V5BCE1, V5BCF5, V5BCG0, V5BCG2, V5BCH0, V5BCH2, V5BCK1, V5BCL4, V5BCM0, V5BCM3, V5BCM4, V5BCN8, V5BCN9, V5BCP2, V5BCP6, V5BCQ8, V5BCS0, V5BCV7, V5BCW9, V5BCZ7, V5BCZ9, V5BD20, V5BD21, V5BD26, V5BD32, V5BD50, V5BD69, V5BD93, V5BDC9, V5BDE1, V5BDF9, V5BDJ7, V5BDK6, V5BDL5, V5BDM6, V5BDQ1, V5BDQ2, V5BDR9, V5BDS9, V5BE13, V5BE31, V5BE86, V5BEB4, V5BEB6, V5BED1, V5BEE7, V5BEF5, V5BEI8, V5BEJ3, V5BEL3, V5BEQ8, V5BER6, V5BEU5, V5BEU6, V5BEV7, V5BEW0, V5BEY7, V5BF02, V5BF06, V5BF20, V5BF34, V5BF44, V5BF59, V5BF65, V5BF76, V5BF86, V5BFC2, V5BFF6, V5BFG1, V5BFG5, V5BFJ0, V5BFM4, V5BFM7, V5BFP9, V5BFS2, V5BFT5, V5BFX1, V5BG00, V5BG02, V5BG04, V5BG05, V5BG13, V5BG30, V5BG34, V5BG41, V5BG46, V5BG78, V5BGC6, V5BGD8, V5BGF1, V5BGF8, V5BGG5, V5BGG8, V5BGH8, V5BGJ6, V5BGL5, V5BGL9, V5BGP0, V5BGQ0, V5BGQ7, V5BGV2, V5BGW0, V5BGX4, V5BH00, V5BH08, V5BH13, V5BH49, V5BH74, V5BH81, V5BH93, V5BHA2, V5BHF5, V5BHI1, V5BHJ6, V5BHK0, V5BHN5, V5BHP4, V5BHP7, V5BHP8, V5BHR5, V5BHU4, V5BHV5, V5BHV8, V5BHZ8, V5BI08, V5BI09, V5BI34, V5BI42, V5BI57, V5BI69, V5BI75, V5BI80, V5BI97, V5BIA7, V5BIC5, V5BIC8, V5BID9, V5BIE9, V5BII1, V5BIL0, V5BIL1, V5BIM5, V5BIP9, V5BIU6, V5BIV9, V5BJ24, V5BJ36, V5BJ41, V5BJ44, V5BJ49, V5BJB5, V5BJC7, V5BJF4, V5BJJ8, V5BJK6, V5BJK7, V5BJL2, V5BJN3, V5BJS7, V5BJU1, V5BJV8, V5BJX4, V5BJY2, V5BJZ6, V5BK17, V5BK30, V5BK31, V5BK60, V5BK64, V5BK66, V5BK67, V5BK86, V5BKA3, V5BKD6, V5BKE4, V5BKF4, V5BKG0, V5BKN5, V5BKN8, V5BKS0, V5BKU4, V5BKV3, V5BKV6, V5BKW2, V5BKW5, V5BL26, V5BL31, V5BL56, V5BL63, V5BL83, V5BLE5, V5BLE8, V5BLF2, V5BLF3, V5BLG8, V5BLI8, V5BLJ2, V5BLJ9, V5BLL2, V5BLM1, V5BLM5, V5BLN7, V5BLQ8, V5BLR7, V5BLS2, V5BLV3, V5BLW0, V5BLX9, V5BLY6, V5BM10, V5BM55, V5BM56, V5BM62, V5BM72, V5BM81, V5BM96, V5BM99, V5BMA7, V5BMG1, V5BMH1, V5BMH6, V5BMI4, V5BMI7, V5BMM9, V5BMN4, V5BMS4, V5BMU5, V5BMW9, V5BMX9, V5BN13, V5BN20, V5BN63, V5BN78, V5BN83, V5BN84, V5BN87, V5BN93, V5BNA2, V5BNF5, V5BNF6, V5BNH8, V5BNJ1, V5BNL9, V5BNN3, V5BNR1, V5BNS0, V5BNS5, V5BNT4, V5BNT6, V5BNU6, V5BNW7, V5BNX4, V5BNZ8, V5BP17, V5BP59, V5BP67, V5BP71, V5BP80, V5BP86, V5BPC4, V5BPE1, V5BPF5, V5BPI7, V5BPJ2, V5BPJ4, V5BPK4, V5BPL8, V5BPQ1, V5BPT0, V5BPT1, V5BPT8, V5BPU0, V5BPU6, V5BPU7, V5BPX6, V5BQ16, V5BQ27, V5BQ29, V5BQ45, V5BQ54, V5BQ71, V5BQA3, V5BQA6, V5BQC9, V5BQD4, V5BQE2, V5BQE9, V5BQF7, V5BQG3, V5BQH3, V5BQI1, V5BQI5, V5BQI6, V5BQJ1, V5BQK1, V5BQK5, V5BQL0, V5BQQ0, V5BQQ6, V5BQR0, V5BQU2, V5BQZ1, V5BR69, V5BR79, V5BR85, V5BRC4, V5BRG3, V5BRH3, V5BRI7, V5BRL1, V5BRP1, V5BRP2, V5BRQ1, V5BRQ8, V5BRQ9, V5BRS6, V5BRU5, V5BRU6, V5BRV7, V5BRY2, V5BRZ5, V5BS79, V5BS80, V5BS87, V5BS95, V5BS99, V5BSA4, V5BSA9, V5BSD2, V5BSD6, V5BSD7, V5BSE1, V5BSE6, V5BSI2, V5BSM8, V5BSN3, V5BSS5, V5BSS7, V5BSW0, V5BSX5, V5BT16, V5BT19, V5BT57, V5BT68, V5BT74, V5BT90, V5BT91, V5BTC6, V5BTG7, V5BTG9, V5BTL3, V5BTM0, V5BTQ6, V5BTR1, V5BTT3, V5BU59, V5BU64, V5BUA6, V5BUD4, V5BUE9, V5BUH4, V5BV01, V5BV18, V5BV36, V5BV46, V5BV57, V5BVI6, V5BVJ1, V5BVK2, V5BVK8, V5BVR2, V5BVU5, V5BVW5, V5BVY2, V5BW01, V5BW18, V5BW22, V5BW37, V5BW71, V5BWB9, V5BWD5, V5BWE0, V5BWE3, V5BWE8, V5BWG3, V5BWH4, V5BWK1, V5BWN0, V5BWN5, V5BWT8, V5BWU3, V5BWX9, V5BWY3, V5BWY7, V5BWZ3, V5BX15, V5BX20, V5BX23, V5BX32, V5BX52, V5BX62, V5BX72, V5BXA0, V5BXB7, V5BXE1, V5BXE5, V5BXF0, V5BXF4, V5BXK2, V5BXR1, V5BXS1, V5BXZ9, V5BY13, V5BY33, V5BY50, V5BY63, V5BYI4, V5BYJ2, V5BYJ7, V5BYK6, V5BYL9, V5BYM3, V5BYM8, V5BYP2, V5BYR2, V5BYV6, V5BYY0, V5BZ53, V5BZN6, V5C089, V5C0D6, V5C1B1, V5C1C6, V5C1F1, V5C1F5, V5C1M1, V5C1Q5, V5C1U9, V5C1Z5, V5C216, V5C230, V5C2S4, V5C2U9, V5C2Y5, V5CHQ8, V5CHW2, V5CWD8, V5D027, V5D050, V5D0C5, V5D0N9, V5D2Y5, V5D3A1, V5D3L3, V5D3X6, V5D424, V5D4J9, V5D4R1, V5D532, V5D5F8, V5D5P0, V5D5S2, V5D631, V5D681, V5D6H5, V5D6I4, V5D725, V5D7G4, V5D7H4, V5D7N3, V5D7P4, V5D7S2, V5D844, V5D881, V5D8D2, V5D8H0, V5D8L4, V5D8P7, V5D8Q5, V5D902, V5D922, V5D930, V5D941, V5D947, V5D9A3, V5D9G5, V5D9U0, V5D9W7, V5D9X8, V5D9Y2, V5DA09, V5DA42, V5DA48, V5DB29, V5DB34, V5DB39, V5DB47, V5DB66, V5DBD1, V5DBG0, V5DBK9, V5DBQ6, V5DBS9, V5DBT5, V5DC73, V5DCD0, V5DCF0, V5DCF9, V5DCP7, V5DCR9, V5DCU5, V5DCV2, V5DCV8, V5DCW6, V5DD41, V5DD63, V5DDD6, V5DDF4, V5DDN3, V5DDP6, V5DDV1, V5DEB6, V5DEM3, V5DES7, V5DFD4, V5DFF3, V5DFK6, V5DFP2, V5DFU6, V5DFV4, V5DG44, V5DGD2, V5DGF4, V5DGN4, V5DGS5, V5DH11, V5DH46, V5DH61, V5DHA5, V5DHJ5, V5DHK1, V5DHL8, V5DHN7, V5DHV0, V5DHW8, V5DHX4, V5DI23, V5DI82, V5DIA0, V5DIB3, V5DIC3, V5DIG4, V5DIQ2, V5DIS6, V5DIT8, V5DIW5, V5DIX7, V5DJ73, V5DJK9, V5DJP6, V5DJS7, V5DJX0, V5DK53, V5DKE1, V5DKQ2, V5DKS4, V5DL00, V5DL46, V5DLC9, V5DLD4, V5DLG6, V5DLI8, V5DLL6, V5DLN7, V5DLP2, V5DLP7, V5DM12, V5DMC3, V5DMK2, V5DMN4, V5DMR8, V5DMS2, V5DMT5, V5DMU2, V5DN37, V5DN54, V5DN77, V5DNT3, V5DNV9, V5DNX2, V5DP62, V5DPC1, V5DPI3, V5DPJ5, V5DPK6, V5DPM8, V5DPU1, V5DQ49, V5DQA0, V5DQB4, V5DQB8, V5DQC0, V5DQD1, V5DQE7, V5DQM2, V5DQS1, V5DQS5, V5DQS9, V5DR98, V5DRE7, V5DRF2, V5DRN5, V5DRY4, V5DS11, V5DSI1, V5DSJ9, V5DSN1, V5DSV1, V5DTE0, V5DTF6, V5DTG5, V5DTI3, V5DTK4, V5DTT7, V5DTU9, V5DU12, V5DU18, V5DU29, V5DUH5, V5DUJ1, V5DUN6, V5DUQ0, V5DUQ5
Leturcq M, Mortuaire M, Hardivillé S, Schulz C, Lefebvre T, Vercoutter-Edouart AS. O-GlcNAc transferase associates with the MCM2-7 complex and its silencing destabilizes MCM-MCM interactions. Cellular and molecular life sciences : CMLS 2018 75(23) 30069701
Abstract:
O-GlcNAcylation of proteins is governed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). The homeostasis of O-GlcNAc cycling is regulated during cell cycle progression and is essential for proper cellular division. We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7. These proteins belong to the MCM2-7 complex which is crucial for the initiation of DNA replication through its DNA helicase activity. Here we show that the six subunits of MCM2-7 are O-GlcNAcylated and that O-GlcNAcylation of MCM proteins mainly occurs in the chromatin-bound fraction of synchronized human cells. Moreover, we identify stable interaction between OGT and several MCM subunits. We also show that down-regulation of OGT decreases the chromatin binding of MCM2, MCM6 and MCM7 without affecting their steady-state level. Finally, OGT silencing or OGA inhibition destabilizes MCM2/6 and MCM4/7 interactions in the chromatin-enriched fraction. In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
O-GlcNAc proteins:
MCM3, MCM4, MCM5, MCM7, MCM2, MCM6
Species: Homo sapiens
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Berthier A, Vinod M, Porez G, Steenackers A, Alexandre J, Yamakawa N, Gheeraert C, Ploton M, Maréchal X, Dubois-Chevalier J, Hovasse A, Schaeffer-Reiss C, Cianférani S, Rolando C, Bray F, Duez H, Eeckhoute J, Lefebvre T, Staels B, Lefebvre P. Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex. Proceedings of the National Academy of Sciences of the United States of America 2018 115(47) 30397120
Abstract:
The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions. An interactomic approach identified O-GlcNAc transferase (OGT) as a REV-ERBα-interacting protein. By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity. We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus. AKT phosphorylation was inversely correlated to REV-ERBα expression. REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites. As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin. Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
O-GlcNAc proteins:
A4D111, POTEF, A5GZ75, AXA2L, P121C, A9Z0R7, EIFCL, C3UMV2, F1JVV5, I6TRR8, MYO1C, IF2B3, DDX3X, TCRG1, OPLA, XPO1, SC16A, SET1A, OGT1, EIF3D, DDX3Y, DHX15, PRP4, SERA, PSMD3, HNRPR, ACTN4, MYO1B, AKAP8, HNRPQ, UGDH, USO1, WDR1, ANR17, GGCT, LX12B, FLNB, PR40A, SF3B1, SPB7, NU155, KRT38, SC24D, GLSK, SC31A, ELP1, SMC2, AGM1, UTS2, BAG4, SC24A, SC24B, AP2A1, LDHA, AL1A1, PGK1, A2MG, CO3, CYTA, KV117, IGHG1, IGHA1, APOE, APOC2, FIBG, TFR1, TRFE, CATA, ALDOA, TBB4A, G3P, HSPB1, RPN1, RPN2, AT1A1, ARGI1, ALDH2, S10A8, ADT2, GELS, ATPB, APOA4, ENOA, PYGL, G6PI, TPM3, PDIA1, CATD, ANXA2, CAN1, TBB5, HS90A, SP1, CO1A2, HS90B, PO2F2, GSTP1, VILI, ANXA4, PARP1, LKHA4, ATX1L, POTEI, UBB, UBC, SAA2, HS71A, HS71B, IGG1, TBA3C, TBA3D, THIO, CH60, BIP, HSP7C, PYGB, PYGM, G6PD, PYC, C1TC, NFH, IMDH2, XRCC6, XRCC5, AT1A3, EF2, PDIA4, P4HA1, ENOB, GFAP, ENPL, IDE, PO2F1, HNRPL, PLAK, DESP, AT2A2, HSP76, DDX5, LEG3, TCPA, RL7, VINC, E2AK2, ITIH2, ANXA7, HNF1A, FILA, CD11B, FLNA, VDAC1, TGM2, PUR2, UBA1, NDKB, TGM1, EST1, SFPQ, SAHH, MCM3, ATPA, PTBP1, SYVC, ABCD3, GRN, TKT, SPB3, AL4A1, PDIA3, KPYR, RPB2, AKT1, PUR9, HNRH1, CASPE, 1433S, S10AB, PRDX2, MCM4, MCM7, HS71L, CTNB1, IRS1, GDE, MYH9, FUS, SPB5, NUP62, TALDO, GRP75, CAPG, TCPZ, STAT3, MDHC, MDHM, ECHA, GARS, SYIC, HUTH, LPPRC, MATR3, MSH2, VDAC2, SYQ, LEG7, COPD, SPB4, TCPE, AL9A1, LMAN1, FMO5, TCPG, SYAC, RBM25, KLK7, DYN2, TCPQ, TCPD, RAB7A, HCFC1, KS6A3, HNRPM, HXK2, CAZA1, NUP98, ACLY, COPB, COPA, SC24C, SYRC, SYYC, UBP14, HSP72, P5CS, XPO2, TERA, MTP, AF17, PSA, HNRH2, EIF3B, SYMC, NU107, EPIPL, TPIS, ACTB, IF4A1, HNRPK, 1433G, PRS4, ACTA, H4, RS27A, RL40, 1433Z, RACK1, ACTG, ACTH, ACTC, ACTS, TBA1B, TBA4A, TBB4B, PRKDC, DCD, VIGLN, CLH1, HNRPU, FABP5, MSHR, EWS, SEMG2, DSG1, SP3, PLOD1, EF1A2, GFPT1, PRDX1, KHDR1, TGM3, DHX9, LG3BP, DSC1, ILF3, TRAP1, PAK2, PSMD2, PABP4, PICAL, PKP1, BLMH, SNTB1, TBB2A, VEZF1, TRI29, UBP2L, LY6D, SRC8, PDIA5, HS902, EPN4, SMC1A, GANAB, MVP, PLEC, NONO, SC23A, SC23B, CDSN, JHD2C, CYTM, DPYL2, PCKGM, TKFC, Q53G76, Q58FF2, Q59EA0, ZN326, FILA2, UBAP2, XP32, RBM26, EF1A3, ARID2, TBA3E, POTEE, SBSN, FBX50, Q70T18, Q71E78, TBA1A, SND1, NUP54, MYH14, PEG10, PRP39, TAXB1, CAND1, CARM1, PRSR1, SPA12, ANKH1, ASXL1, NUP93, RDHE2, Q8N6B4, PDPR, TNR6A, COP1, PDC6I, POF1B, ATX2L, DDX1, BAP1, TFG, RBP56, EVPL, DDX17, RENT1, FUBP2, UBP7, NCLN, H2B1A, WNK4, ZC3HA, SCYL1, SPB12, GSDMA, VPS35, PHF12, CIC, STRBP, VAT1, NUP88, ATX2, CPNE1, TCPH, TBA1C, DIDO1, HNRL1, TBB2B, NUP58, ACTBM, TB182, SP130, WNK1, AGO3, MCCB, MOV10, TNR6C, S10AE, DD19A, ATD3A, TBA8, UGGG1, IF2B1, CALL5, RRBP1, NXF1, CMC2, PO2F3, AGO2, AGO1, Q9UL79, ACSL5, DD19B, TNR6B, CD11A, EIF3L, SYFA, KLK5, RTCB, WNK2, PKP3, HYOU1, SNX9, COPG1, IF2B2, S23IP
Species: Homo sapiens
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Aquino-Gil MO, Kupferschmid M, Shams-Eldin H, Schmidt J, Yamakawa N, Mortuaire M, Krzewinski F, Hardivillé S, Zenteno E, Rolando C, Bray F, Pérez Campos E, Dubremetz JF, Perez-Cervera Y, Schwarz RT, Lefebvre T. Apart From Rhoptries, Identification of Toxoplasma gondii's O-GlcNAcylated Proteins Reinforces the Universality of the O-GlcNAcome. Frontiers in endocrinology 2018 9 30177911
Abstract:
O-linked β-N-acetylglucosaminylation or O-GlcNAcylation is a widespread post-translational modification that belongs to the large and heterogeneous group of glycosylations. The functions managed by O-GlcNAcylation are diverse and include regulation of transcription, replication, protein's fate, trafficking, and signaling. More and more evidences tend to show that deregulations in the homeostasis of O-GlcNAcylation are involved in the etiology of metabolic diseases, cancers and neuropathologies. O-GlcNAc transferase or OGT is the enzyme that transfers the N-acetylglucosamine residue onto target proteins confined within the cytosolic and nuclear compartments. A form of OGT was predicted for Toxoplasma and recently we were the first to show evidence of O-GlcNAcylation in the apicomplexans Toxoplasma gondii and Plasmodium falciparum. Numerous studies have explored the O-GlcNAcome in a wide variety of biological models but very few focus on protists. In the present work, we used enrichment on sWGA-beads and immunopurification to identify putative O-GlcNAcylated proteins in Toxoplasma gondii. Many of the proteins found to be O-GlcNAcylated were originally described in higher eukaryotes and participate in cell shape organization, response to stress, protein synthesis and metabolism. In a more original way, our proteomic analyses, confirmed by sWGA-enrichment and click-chemistry, revealed that rhoptries, proteins necessary for invasion, are glycosylated. Together, these data show that regardless of proteins strictly specific to organisms, O-GlcNAcylated proteins are rather similar among living beings.
O-GlcNAc proteins:
A0A0F7UNS7, A0A0F7UNS9, A0A0F7US18, A0A0F7USN9, A0A0F7UTC9, A0A0F7UTU3, A0A0F7UU04, A0A0F7UUK6, A0A0F7UVN4, A0A0F7UY31, A0A0F7UZ13, A0A0F7UZH2, A0A0F7UZN1, A0A0F7V117, A0A0F7V1A1, A0A0F7V207, A0A0F7V2H9, A0A0F7V4E5, A0A0F7V4M1, A0A0F7V4V1, A0A0F7V5E7, A0A0F7V6C1, A0A0F7V6Y1, A0A0F7V8D8, A0A0F7V8D9, A0A0F7V9A2, A0A0F7VAM4, A0A0F7VDV9, A0A0F7VFL4, A0A125YFT6, A0A125YH03, A0A125YH19, A0A125YH31, A0A125YIG1, A0A125YII2, A0A125YIQ1, A0A125YJ41, A0A125YJA7, A0A125YJY9, A0A125YK30, A0A125YK31, A0A125YKA6, A0A125YKH1, A0A125YKP3, A0A125YLH3, A0A125YMU1, A0A125YMW2, A0A125YNJ7, A0A125YNX2, A0A125YQ71, A0A125YQT4, A0A125YQU5, A0A125YQZ2, A0A125YR71, A0A125YRV5, A0A125YSE3, A0A125YSL8, A0A125YST2, A0A125YSX9, A0A125YT22, A0A125YTY5, A0A125YU34, A0A125YUA7, A0A125YUK5, A0A125YV47, A0A125YVI3, A0A125YVX3, A0A125YWA4, A0A125YWN6, A0A125YWW1, A0A125YWX7, A0A125YXF0, A0A125YXW4, A0A125YXY8, A0A125YYA8, A0A125YYN8, A0A125YYR2, A0A125YZB5, B6K8J7, B6K8K4, B6K8L1, B6K8Q8, B6K8Y9, B6K9E4, B6K9Y2, B6K9Z3, B6KA38, B6KA89, B6KAE3, B6KAG9, B6KAL4, B6KAM8, B6KAW0, B6KAW1, B6KB01, B6KB03, B6KB88, B6KBA7, B6KDL6, B6KDN4, B6KFE8, B6KFK7, B6KGK3, B6KGN5, B6KH13, B6KH90, B6KHU4, B6KJ68, B6KJD0, B6KJP5, B6KJX9, B6KKZ7, B6KL08, B6KM09, B6KNZ3, B6KP76, B6KR20, B6KRA7, B6KT39, B6KT44, B6KVA6, B9PFX5, B9PGG2, B9PGZ9, B9PH46, B9PHN7, B9PIA4, B9PIV3, B9PIY5, B9PJA8, B9PJD4, B9PJM1, B9PK53, B9PKF7, B9PKL4, B9PKM9, B9PL62, B9PLD0, B9PLQ7, B9PM19, B9PM93, B9PMK8, B9PMK9, B9PMN6, B9PMU7, B9PMV3, B9PMV8, B9PMX8, B9PMZ3, B9PN66, B9PNK6, B9PNS2, B9PP49, B9PPK8, B9PPQ1, B9PPQ9, B9PQM0, B9PQR4, B9PRA3, B9PRA8, B9PRN1, B9PS36, B9PSW9, B9PSX1, B9PT01, B9PT27, B9PT75, B9PTC2, B9PTE8, B9PTM6, B9PTX0, B9PTZ1, B9PU09, B9PU56, B9PU99, B9PUJ6, B9PUM9, B9PV52, B9PVR5, B9PVZ6, B9PW44, B9PW48, B9PWK0, B9PWN3, B9PWQ2, B9PX11, B9PXE4, B9PXJ3, B9PYA4, B9PYC5, B9PYN1, B9PYS5, B9PYV2, B9PYW7, B9PZC9, B9PZF2, B9PZG9, B9PZT4, B9PZU5, B9Q018, B9Q055, B9Q0C6, B9Q0N7, B9Q0Q9, B9Q199, B9Q1T8, B9Q363, B9Q3S1, B9Q3U3, B9Q5A4, B9Q5R8, B9Q605, B9Q788, B9Q7L9, B9Q7W2, B9Q7Y3, B9Q8A2, B9QAU9, B9QAY6, B9QB60, B9QC07, B9QEH5, B9QFB6, B9QFR6, B9QFV9, B9QFW3, B9QH60, B9QHF5, B9QHQ6, B9QHX6, B9QJ78, B9QJK9, B9QJS4, B9QK32, B9QLU2, B9QMJ0, B9QML2, B9QMZ2, B9QND8, B9QP57, B9QP69, B9QPA4, B9QPM2, B9QPQ2, B9QR10, B9QR35, B9QR64, V4YI32, V4YI37, V4YID2, V4YPG9, V4YQV9, V4YTV2, V4YVI5, V4YW47, V4YXJ8, V4YY60, V4YYL5, V4YYT6, V4YZ17, V4Z117, V4Z2A3, V4Z301, V4Z362, V4Z3K0, V4Z409, V4Z481, V4Z6M2, V4Z6U4, V4Z6U8, V4Z712, V4Z806, V4Z8G0, V4Z8Z4, V4Z9B7, V4Z9F7, V4Z9I7, V4Z9M8, V4ZA01, V4ZBD9, V4ZD29, V4ZD64, V4ZD88, V4ZDB0, V4ZE39, V4ZF64, V4ZFG5, V4ZIR0, V4ZR02, V5AWC8, V5AWD9, V5AWM3, V5AXL6, V5B218, V5B2A1, V5B2X9, V5B518, V5B5J6, V5B6B7, V5BCJ1, V5BD96, V5BDD5, V5BDM3, V5BF03, V5BFN0
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Kupferschmid M, Aquino-Gil MO, Shams-Eldin H, Schmidt J, Yamakawa N, Krzewinski F, Schwarz RT, Lefebvre T. Identification of O-GlcNAcylated proteins in Plasmodium falciparum. Malaria journal 2017 16(1) 29187233
Abstract:
Post-translational modifications (PTMs) constitute a huge group of chemical modifications increasing the complexity of the proteomes of living beings. PTMs have been discussed as potential anti-malarial drug targets due to their involvement in many cell processes. O-GlcNAcylation is a widespread PTM found in different organisms including Plasmodium falciparum. The aim of this study was to identify O-GlcNAcylated proteins of P. falciparum, to learn more about the modification process and to understand its eventual functions in the Apicomplexans.
O-GlcNAc proteins:
KC1, HSP70, ALF, TBA, PGK, CH60, EF1A, HXK, BIP, OAT, ENO, ACT1, ACT2, MYOA
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Baldini SF, Steenackers A, Olivier-Van Stichelen S, Mir AM, Mortuaire M, Lefebvre T, Guinez C. Glucokinase expression is regulated by glucose through O-GlcNAc glycosylation. Biochemical and biophysical research communications 2016 478(2) 27520373
Abstract:
Blood glucose fluctuates with the fasting-feeding cycle. One of the liver's functions is to maintain blood glucose concentrations within a physiological range. Glucokinase (GCK) or hexokinase IV, is the main enzyme that regulates the flux and the use of glucose in the liver leading to a compensation of hyperglycemia. In hepatocytes, GCK catalyzes the phosphorylation of glucose into glucose-6-phosphate. This critical enzymatic reaction is determinant for the metabolism of glucose in the liver which includes glycogen synthesis, glycolysis, lipogenesis and gluconeogenesis. In liver, simultaneous increase of glucose and insulin enhances GCK activity and gene expression, changes its subcellular location and interaction with regulatory proteins. The post-translational O-linked β-N-acetylglucosaminylation (O-GlcNAcylation) acts as a glucose-sensitive modification and is believed to take part in hepatic glucose sensing by modifying key regulatory proteins. Therefore, we aimed to determine whether GCK is modified by O-GlcNAcylation in the liver of mice and investigated the role that this modification plays in regulating GCK protein expression. We demonstrated that endogenous GCK expression correlated with O-GlcNAc levels in the pathophysiological model ob/ob mice. More specifically, in response to the pharmacological inhibition of O-GlcNAcase (OGA) contents of GCK increased. Using the GlcNAc specific lectin succinylated-WGA and click chemistry labeling approaches, we demonstrated that GCK is modified by O-GlcNAcylation. Further, we demonstrated that siRNA-mediated Ogt knock-down not only decreases O-GlcNAc content but also GCK protein level. Altogether, our in vivo and in vitro results demonstrate that GCK expression is regulated by nutrient-sensing O-GlcNAc cycling in liver.
O-GlcNAc proteins:
HXK4
Species: Mus musculus
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Baldini SF, Wavelet C, Hainault I, Guinez C, Lefebvre T. The Nutrient-Dependent O-GlcNAc Modification Controls the Expression of Liver Fatty Acid Synthase. Journal of molecular biology 2016 428(16) 27185461